Role of the mitogen‐activated protein kinases and tyrosine kinases during leukotriene B4‐induced eosinophil activation

Exposure of guinea‐pig eosinophils to leukotriene B4 (LTB4; 1 μM) resulted in a rapid generation of H2O2 (index of NADPH oxidase activation), stimulated [3H]arachidonic acid (AA) release (index of phospholipase A2 activity), and promoted CD18‐dependent homotypic aggregation. Under similar conditions, LTB4 (1 μM) induced a rapid activation of extracellular‐regulated kinases‐1 and 2 (ERK‐1/2) but not c‐jun N‐terminal kinases 46 and 54 (JNK‐46/54) or p38 mitogen‐activated protein kinase (p38 MAP kinase). To examine the role of ERK‐1/2 in the mechanism of eosinophil activation, a selective inhibitor of MAP kinase kinase‐1/2 (MEK‐1/2), PD098059, was employed. However, PD 098059 at concentrations that attenuated ERK‐1/2 activation had no significant affect on eosinophil activation. In contrast, a role for tyrosine kinases in LTB4‐induced eosinophil activation was suggested by studies with the tyrosine kinase inhibitors, herbimycin A and lavendustin A. However, the results of those experiments implied divergent pathways for the control of eosinophil responses because the inhibitors were more effective at attenuating H2O2 generation than [3H]AA release, and had little effect on homotypic aggregation. J. Leukoc. Biol. 64: 555–562; 1998.

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